Human cytomegalovirus packaging: an update on structure–function relationships

Abstract

DNA packaging of human cytomegalovirus is a key step in viral replication. Enzymes required for this process are the terminase subunits pUL56 and pUL89. Together with the portal protein, pUL104, they form a powerful biological nanomotor. It has been demonstrated that for tailed dsDNA bacteriophages, DNA translocation into preformed capsid needs an extraordinary amount of energy. The terminase subunit pUL56 provides the required ATP-hydrolyzing activity for DNA packaging. The necessary nuclease activity to process the concatemers into unit-length genomes is mediated by the terminase subunit pUL89. The ring-like structure of both terminase subunits is in concordance with their function as DNA-metabolizing proteins. Binding to the portal is a prerequisite for DNA translocation into the capsid. The latest models suggest that the terminase moves along some domains of the DNA by a binding and release mechanism.